Evaluation of the Structure and Conformation of Albumin Protein after Interaction with Graphene and Graphene Oxide

Abstract

Given the increasing demand for graphene-based nanomaterials, it seems necessary to study their effects on the biomolecules they encounter. In this study, we will present the results of our computational study on the influence of graphene and graphene oxide (GO) on albumin. The interaction between albumin, graphene and GO was investigated using molecular dynamics and GROMACS software for 100 ns with a TIP3P water model. Binding energy, its root-mean-square deviation and structural changes were calculated. The molecular dynamics results show that the interaction of albumin with both graphene and GO structures causes changes in protein structure and that GO has a larger effect on the secondary structure. The results show that the binding energy between albumin and graphene is higher than that of GO. The analysis shows that it is more related to non-polar or hydrophobic interactions in the albumin-graphene interaction. Graphene and GO affect the protein microenvironment and reduce the amount of secondary structure, but in general the degree of change depends on the ratio of graphene or GO to albumin, GO functional groups, temperature and pH.